ID D1BEV7_SANKS Unreviewed; 238 AA. AC D1BEV7; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000256|HAMAP-Rule:MF_00421}; DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00421}; DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00421}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000256|HAMAP-Rule:MF_00421}; DE Short=FGAR amidotransferase I {ECO:0000256|HAMAP-Rule:MF_00421}; DE Short=FGAR-AT I {ECO:0000256|HAMAP-Rule:MF_00421}; DE AltName: Full=Glutaminase PurQ {ECO:0000256|HAMAP-Rule:MF_00421}; DE EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_00421}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000256|HAMAP-Rule:MF_00421}; GN Name=purQ {ECO:0000256|HAMAP-Rule:MF_00421}; GN OrderedLocusNames=Sked_35050 {ECO:0000313|EMBL:ACZ23393.1}; OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae; OC Sanguibacter. OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ23393.1, ECO:0000313|Proteomes:UP000000322}; RN [1] {ECO:0000313|EMBL:ACZ23393.1, ECO:0000313|Proteomes:UP000000322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74 RC {ECO:0000313|Proteomes:UP000000322}; RX PubMed=21304646; RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C., RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A., RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R., RA Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74)."; RL Stand. Genomic Sci. 1:110-118(2009). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes the CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and CC glutamate. The FGAM synthase complex is composed of three subunits. CC PurQ produces an ammonia molecule by converting glutamine to glutamate. CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- CC dependent manner. PurS interacts with PurQ and PurL and is thought to CC assist in the transfer of the ammonia molecule from PurQ to PurL. CC {ECO:0000256|HAMAP-Rule:MF_00421}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D- CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00421}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00421}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00421}. CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ CC and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00421}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00421}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001819; ACZ23393.1; -; Genomic_DNA. DR RefSeq; WP_012868461.1; NC_013521.1. DR AlphaFoldDB; D1BEV7; -. DR STRING; 446469.Sked_35050; -. DR KEGG; ske:Sked_35050; -. DR eggNOG; COG0047; Bacteria. DR HOGENOM; CLU_001031_3_1_11; -. DR OrthoDB; 9804441at2; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000322; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01740; GATase1_FGAR_AT; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00421; PurQ; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ. DR NCBIfam; TIGR01737; FGAM_synth_I; 1. DR PANTHER; PTHR47552; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1. DR PANTHER; PTHR47552:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1. DR Pfam; PF13507; GATase_5; 1. DR PIRSF; PIRSF001586; FGAM_synth_I; 1. DR SMART; SM01211; GATase_5; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00421}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00421}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_00421}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00421}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00421}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00421}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_00421}. FT ACT_SITE 92 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 201 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 203 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00421, FT ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 238 AA; 24941 MW; BD8DB58913F80F73 CRC64; MSDVLTGARI GVITFPGTLD DRDAARAVRI AGATAVPLWH ADADLHGVDA VVLPGGFSYG DYLRAGAISR FAPVMDVLVD AAKGGLPVLG ICNGFQILTE SHLLPGSMIK NDSLSFLCRE QRLTVENADT AWTRGFRAGQ EITIPLKNQD GQFVADEHTL DELEGEGRVV FRYAGENPNG SRRGIAGITN AAGNVVGLMP HPEHAVEVGF GTAAEAGPRA GTDGLTFFTS VLGTLVTA //